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Bond-Mediated Electron Tunneling in Ruthenium-Modified High-Potential Iron−Sulfur Protein

Babini, Elena and Bertini, Ivano and Borsari, Marco and Capozzi, Francesco and Luchinat, Claudio and Zhang, Xiaoyu and Moura, Gustavo L. C. and Kurnikov, Igor V. and Beratan, David N. and Ponce, Adrian and Di Bilio, Angel J. and Winkler, Jay R. and Gray, Harry B. (2000) Bond-Mediated Electron Tunneling in Ruthenium-Modified High-Potential Iron−Sulfur Protein. Journal of the American Chemical Society, 122 (18). pp. 4532-4533. ISSN 0002-7863. doi:10.1021/ja994472t.

[img] PDF (Ruthenium modification procedure; absorption spectra; electrochemical procedure, voltammograms, and reduction potentials for HiPIP and Ru(His42)HiPIP (Ru3+/2+ and Fe3+/2+ couples) measured at eight different temperatures; HiPIP and ruthenium difference ab) - Supplemental Material
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High-potential iron−sulfur proteins (HiPIPs) are found in photosynthetic purple nonsulfur bacteria. The three-dimensional structure of Chromatium vinosum HiPIP features two short segments of α-helix, three strands of antiparallel β-pleated sheet, and a small helix near the N-terminus. The cubane [Fe_4S_4] cluster is attached covalently to the polypeptide matrix through Fe−S^γ bonds to cysteines 43, 46, 63, and 77. The side chains of Tyr19, Phe48, Trp60, Phe66, Trp76, Trp80, and other nonpolar residues encapsulate the cluster in a hydrophobic cavity that is inaccessible to solvent. Tyr19, which contacts the [Fe_4S_4] core, has been suggested to play a particularly important structural role. In both oxidation states, the cysteinyl and core inorganic sulfur atoms are involved in H-bonding interactions with peptide NH protons.

Item Type:Article
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URLURL TypeDescription Information
Winkler, Jay R.0000-0002-4453-9716
Gray, Harry B.0000-0002-7937-7876
Additional Information:© 2000 American Chemical Society. Received December 22, 1999. Publication Date (Web): April 22, 2000. We thank Brian Crane for helpful discussions. This research was supported by NIH (DK19038 to H.B.G.; GM48043 to D.N.B.), the Howard Hughes Medical Institute (summer undergraduate research fellowship to X.Z.), and CAPES-Brazil (graduate fellowship to G.L.C.M.).
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Howard Hughes Medical Institute (HHMI)UNSPECIFIED
Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)UNSPECIFIED
Issue or Number:18
Record Number:CaltechAUTHORS:20170421-092308907
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Official Citation:Bond-Mediated Electron Tunneling in Ruthenium-Modified High-Potential Iron−Sulfur Protein Elena Babini, Ivano Bertini, Marco Borsari, Francesco Capozzi, Claudio Luchinat, Xiaoyu Zhang, Gustavo L. C. Moura, Igor V. Kurnikov, David N. Beratan, Adrian Ponce, Angel J. Di Bilio, Jay R. Winkler, and, and Harry B. Gray, Journal of the American Chemical Society 2000 122 (18), 4532-4533 DOI: 10.1021/ja994472t
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:76809
Deposited By: Tony Diaz
Deposited On:21 Apr 2017 18:12
Last Modified:15 Nov 2021 17:02

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